Phenoloxidase in the scallop Chlamys farreri: Purification and antibacterial activity of its reaction products generated in vitro

Xing, Jing; Jiang, Jingwei; Zhan, Wenbin

doi:10.1016/j.fsi.2011.10.025

Cited by 21 publications

(6 citation statements)

References 40 publications

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“…Similar antibacterial activity was reported in the haemolymph of Pacific oyster C. gigas, but it was considered to be mainly derived from the laccase [12]. Very recently, a phenoloxidase was isolated and purified from scallop C. farreri with antibacterial activity [44]. These antibacterial functions were suspected to be derived from some reactive intermediate substrates such as o-quinones and DHI produced in the catalysis reaction of phenoloxidases, because these reactive intermediate substances displayed broad-spectrum antibacterial and antifungal activities in arthropod [17,18,45,46].…”

Section: Discussionsupporting

confidence: 57%

The phenoloxidase activity and antibacterial function of a tyrosinase from scallop Chlamys farreri

Zhou

Wang

et al. 2012

Fish & Shellfish Immunology

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Section: Discussionsupporting

confidence: 57%

The phenoloxidase activity and antibacterial function of a tyrosinase from scallop Chlamys farreri

Zhou

Wang

et al. 2012

Fish & Shellfish Immunology

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“…Here, we observed that the purified recombinant MpPO protein inhibited the growth of V. parahaemolyticus and S. aureus (Figures 6, 7). This was consistent with the notion that PO could inhibit the growth of Vibrio in the scallop Chlamys farreri , discussed previously by Xing et al (40). Bacterial growth inhibition was also observed in the presence of PO in Crassostrea gigas (41).…”

Section: Discussionsupporting

confidence: 93%

MITF Regulates Downstream Genes in Response to Vibrio parahaemolyticus Infection in the Clam Meretrix Petechialis

Zhang

Yue

et al. 2019

Front. Immunol.

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The microphthalmia-associated transcription factor (MITF) is a basic helix-loop-helix-leucine zipper protein that plays a key role in cell proliferation, survival and immune defense through the direct transcriptional control of downstream genes. We have found that MITF participates in the immune response to Vibrio parahaemolyticus infection in the clam Meretrix petechialis . In this study, we focused on how MITF functions in immunity. First, PO, CTSK , and BCL-2 were identified as the target genes of MpMITF in the clam by RNAi. EMSAs showed direct binding between the MpMITF protein and the E-box of the MpPO, MpCTSK , and MpBCL-2 promoters. Yeast one-hybrid assays also suggested that MpMITF could activate the expression of these three downstream genes. These results demonstrated that the transcriptional expression of MpPO, MpCTSK , and MpBCL-2 is directly regulated by MpMITF. Second, we analyzed the roles of MpPO, MpCTSK , and MpBCL-2 in clam immunity. The mRNA expression of MpPO, MpCTSK , and MpBCL-2 increased significantly after V. parahaemolyticus challenge, which implied that these genes might take part in the immune defense against V. parahaemolyticus challenge in clams. The purified recombinant proteins, MpPO and MpCTSK, inhibited the growth of V. parahaemolyticus . Additionally, the apoptosis rate of clam haemocytes rose significantly when the activity of MpBCL-2 was suppressed. These results revealed that MpPO, MpCTSK , and MpBCL-2 are involved in the immune defense against V. parahaemolyticus . This study supports the idea that the MpMITF pathway plays a key role in immune defense through the direct regulation of the downstream genes MpPO, MpCTSK , and MpBCL-2 in the clam, M. petechialis .

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“…Mollusc and arthropod hemocyanins (Hcs) contribute in many ways to immune defences, such as the inhibition of viral replication, the liberation of AMPs, and the conformational switch to a PO-like enzyme (reviewed by Coates and Nairn, 2014). Reaction products from crustacean (Cerenius et al 2010;Charoensapsri et al, 2014), insect (Zhao et al, 2007) and bivalve (Xing et al, 2012) POs in the presence of dopamine and/or L -DOPA can agglutinate and kill microbes, including the vertebrate pathogens Candida albicans and Vibrio parahaemolyticus (Table 2). Such reactive by-products tend to be oxidising (e.g.…”

Section: Discussionmentioning

confidence: 99%

Hemocyanin-derived phenoloxidase reaction products display anti-infective properties

Coates

Talbot

2018

Developmental & Comparative Immunology

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Hemocyanin is a multi-functional protein located in the hemolymph (blood) of certain arthropods and molluscs. In addition to its well-defined role in oxygen transport, hemocyanin can be converted into a phenoloxidase-like enzyme. Herein, we tested the antimicrobial properties of horseshoe crab (Limulus polyphemus) hemocyanin-derived phenoloxidase reaction products using broad ranges of phenolic substrates (e.g. -DOPA) and microbial targets (Gram-positive/negative bacteria, yeast). The enzyme-catalysed turnover of several substrates generated (by)products that reduced significantly the number of colony forming units. Microbicidal effects of hemocyanin-derived phenoloxidase were thwarted by the inhibitor phenylthiourea. Data presented here further support a role for hemocyanin in invertebrate innate immunity.

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Phenoloxidase in the scallop Chlamys farreri: Purification and antibacterial activity of its reaction products generated in vitro

Cited by 21 publications

References 40 publications

The phenoloxidase activity and antibacterial function of a tyrosinase from scallop Chlamys farreri

The phenoloxidase activity and antibacterial function of a tyrosinase from scallop Chlamys farreri

MITF Regulates Downstream Genes in Response to Vibrio parahaemolyticus Infection in the Clam Meretrix Petechialis

Hemocyanin-derived phenoloxidase reaction products display anti-infective properties

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